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Relevant bibliographies by topics / Erythrocruorins

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Academic literature on the topic 'Erythrocruorins'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "Erythrocruorins"

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Musmeci, M. Teresa, and Vincenzo D'Amelio. "Erythrocruorin subunits ofPerinereis cultriferaGrube (Annelida, Polychaeta) compared with other erythrocruorins." Bolletino di zoologia 52, no. 3-4 (1985): 211–17. http://dx.doi.org/10.1080/11250008509440520.

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Hendrickson, W. A., and W. E. Royer. "Principles in the assembly of annelid erythrocruorins." Biophysical Journal 49, no. 1 (1986): 177–89. http://dx.doi.org/10.1016/s0006-3495(86)83633-5.

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Vinogradov, Serge N. "The structure of invertebrate extracellular hemoglobins (erythrocruorins and chlorocruorins)." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 82, no. 1 (1985): 1–15. http://dx.doi.org/10.1016/0305-0491(85)90120-8.

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Zimmerman, Devon, Matthew DiIusto, Jack Dienes, Osheiza Abdulmalik, and Jacob J. Elmer. "Direct comparison of oligochaete erythrocruorins as potential blood substitutes." Bioengineering & Translational Medicine 2, no. 2 (2017): 212–21. http://dx.doi.org/10.1002/btm2.10067.

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KLEINSCHMIDT, Traute, Hans-Günther KEYL, and Gerhard BRAUNITZER. "Comparison of Insect Hemoglobins (Erythrocruorins) fromChironomus thummi thummiandChironomus thummi piger (Diptera).The Primary Structure of the Monomeric Hemoglobin CTP III." Biological Chemistry Hoppe-Seyler 370, no. 2 (1989): 839–46. http://dx.doi.org/10.1515/bchm3.1989.370.2.839.

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Bridges, C. R., and S. Morris. "Respiratory pigments: interactions between oxygen and carbon dioxide transport." Canadian Journal of Zoology 67, no. 12 (1989): 2971–85. http://dx.doi.org/10.1139/z89-420.

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Oxygen and carbon dioxide are transported in vertebrates and invertebrates by a wide range of respiratory pigments. These respiratory gases are not transported independently of one another, and this review considers the influence of carbon dioxide on oxygen transport and vice versa. A specific effect of carbon dioxide or bicarbonate, decreasing oxygen affinity, is found in many haemoglobins, but the effect is often reduced in the presence of organic phosphates. Clear experimental data are available for mammalian haemoglobins but in birds and lower vertebrates more data are required to verify the presence and magnitude of the CO2 effect. In erythrocruorins and haemocyanins CO2 increases O2 affinity, whereas in haemerythrins, as in haemoglobin, CO2 again decreases oxygen affinity. Much of our knowledge of invertebrate respiratory pigments is based, however, on data from one or two species. A specific effect of CO2 on O2 affinity has also often been found only at high CO2 partial pressures, which may be outside the physiological range for these species. More in vivo experimental data on CO2 values are required for these species, and further studies on other species may help to explain this discrepancy. The interaction of O2 and CO2 transport is mainly through the Haldane effect, i.e., deoxygenated blood having a greater capacity for CO2 than oxygenated blood. This is due directly to the formation of carbamino groups (carbamate) and also to the fact that deoxygenated blood binds relatively more protons than oxygenated blood. This forms the basis for the linkage between the Bohr and Haldane effects. In some species in which the Bohr coefficient is below −1.0, an akalosis in the tissues may be induced. Large Haldane effects may be particularly effective in promoting CO2 unloading when the partial pressure difference of CO2 between arterial and venous blood is small. Carbamate formation may account for 10–20% of the CO2 transported in mammals, but its role in lower vertebrates and invertebrates has only recently been considered. Carbon dioxide transport is modulated by those factors that influence O2 affinity as these in turn influence the Haldane effect.

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Darawshe, S., Y. Tsafadyah, and E. Daniel. "Quaternary structure of erythrocruorin from the nematode Ascaris suum. Evidence for unsaturated haem-binding sites." Biochemical Journal 242, no. 3 (1987): 689–94. http://dx.doi.org/10.1042/bj2420689.

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The quaternary structure of erythrocruorin from the nematode Ascaris suum was studied. The native protein had a sedimentation coefficient, at a protein concentration of 1 mg/ml, of 11.6 +/- 0.3 S and an Mr, as determined by sedimentation equilibrium, of 332,000 +/- 17,000. SDS/polyacrylamide-gel electrophoresis gave one band with a mobility corresponding to an Mr of 43,000 +/- 2000. The Mr of the polypeptide chain was determined to be 41,600 +/- 1,500 by sedimentation equilibrium in 6 M-guanidinium chloride and 0.1 M-2-mercaptoethanol. Cross-linking with glutaraldehyde followed by SDS/polyacrylamide-gel electrophoresis yielded a maximal number of eight bands. The haem content of Ascaris erythrocruorin was observed to vary from one preparation to another. This finding was shown to be due to non-realization of the full binding capacity for haem. By titration with haemin, the haem content was found to attain a maximal value of 2.86 +/- 0.14%, corresponding to a minimal Mr per haem group of 21,000 +/- 1,000. Our findings indicate that Ascaris suum erythrocruorin is composed of eight identical polypeptide chains, carrying two haem sites each.

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Royer, William E., Wayne A. Hendrickson, and Warner E. Love. "Crystals of Lumbricus erythrocruorin." Journal of Molecular Biology 197, no. 1 (1987): 149–53. http://dx.doi.org/10.1016/0022-2836(87)90618-8.

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Royer, W. E., and W. A. Hendrickson. "Molecular symmetry of Lumbricus erythrocruorin." Journal of Biological Chemistry 263, no. 27 (1988): 13762–65. http://dx.doi.org/10.1016/s0021-9258(18)68307-3.

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Strand, K., and W. Royer Jr. "Crystallographic investigations of erythrocruorin fromLumbricus terrestris." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C178. http://dx.doi.org/10.1107/s0108767396092185.

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Dissertations / Theses on the topic "Erythrocruorins"

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Bhanumathy, M. "Studies on invertebrate erythrocruorins : A structural kinetic and spectroscopic investigation." Thesis, University of Essex, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356045.

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Bachega, José Fernando Ruggiero. "Estrutura cristalográfica da hemoglobina gigante de Glossoscolex paulistus, um complexo de 3,6 mega Daltons." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-22082013-153157/.

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Eritrocruorinas são hemoglobinas gigantes compostas por uma bicamada hexagonal de massa molecular total entre 3,0 e 4,0 MDa. A sua estrutura é baseada em unidades básicas chamadas protômeros. Doze destes compõem a partícula inteira, seis em cada camada hexagonal, resultando numa estrutura contendo 180 subunidades. Nas eritrocruorinas do tipo I, o protômero é constituído por quatro tipos de cadeias de globina: a, b, c, e d, e por três tipos de cadeias de linkers, L1, L2 e L3. A compreensão atual do seu mecanismo da ação esta atualmente prejudicada pela resolução limitada das estruturas cristalográficas disponíveis. Para abordar esta questão procuramos cristalizar uma serie de eritrocruorinas de espécies diversas visando a determinação das suas estruturas a mais alta resolução. Na primeira parte deste trabalho a eritrocruorina de Glossoscolex paulistus (HbGp) teve suas subunidades sequenciadas e a estrutura da partícula inteira resolvida a uma resolução de 3,2Å, a mais alta até o momento. Na estrutura da HbGp as quatro cadeias de globina se associam na forma de um heterotetrâmero, que se repete três vezes formando uma estrutura dodecamérica denominada cap. A estrutura do cap associada a um heterotrímero de linkers forma o então mencionado protômero. A estrutura completa permite uma descrição mais detalhada dos contatos entre subunidades que são essenciais para a manutenção da partícula como um todo. Além disto descrevemos sítios de ligação a metais (Zn2+ e Ca2+) e sítios de glicosilação, alguns dos quais são inéditos. Em seguida, a subunidade d isolada da HbGp foi cristalizada e resolvida a 2.1Å. Uma analise dos contatos cristalinos demonstra um arranjo completamente diferente daquilo visto para a subunidade d no complexo inteira. Ao invés de associar-se na formar trimeros, como acontece no complexo, a cadeia d isolada forma dímeros cristalográficos, com interface similar a aquela observada entre as cadeias d e a. Estas observações contribuíram para a compreensão de como são os possíveis mecanismos de associação das globinas para a montagem do cap. Finalmente, as eritrocruorinas de quatro outras espécies foram cristalizadas, que resultou na obtenção de uma estrutura cristalográfica preliminar para a eritrocruorina de Eisenia Andrei a uma resolução de 4.7Å.<br>Erythrocruorins are giant haemoglobins in the form of a hexagonal bilayer of total molecular mass between 3 and 4 MDa. Their structures are based on a basic unit called the protomer. Twelve of these comprise the entire particle, six in each hexagonal layer, resulting in a structure containing 180 subunits. In the type I erythrocruorins the protomer is composed of four types of globin chains: a, b, c e d, and three types of linker; L1, L2 e L3. Our current understanding of their mechanism of action is limited by the resolution of the crystal structures available. To address this question we have attempted to crystallize a series of erythrocruorins from different species with a view to determining a crystal structure at higher resolution. In the first part of this thesis all chains of the erythrocruorin from Glossoscolex paulistus were completely sequenced and the structure of the full particle solved at 3.2Å, the highest reported to date. In the structure the four globin chains associate to form a heterotetramer, three of which unite to form a dodecameric cap. The latter associates with a heterotrimer of linkers to form the aforementioned protomer. The full structure permits a more detailed description of the contacts between subunits which are essential for particle stability. Furthermore, we describe metal binding sites (Zn2+ e Ca2+) and glycosylation sites, some of which are have not been reported previously. Subsequently the isolated d chain was crystallized and solved to 2.1Å. An analysis of the crystal contacts shows an arrangement which is completely different to that seen in the full particle. Instead of forming trimers, as seen in the complex, the isolated d chain associates to form a dimer across a crystallographic twofold axis making use of the interface normally used to associate with subunit a. These observations contributed to our understanding of the possible mechanisms of association of globin chains during the formation of the cap. Finally, the erythrocruorins from four other species were crystallized, which resulted in the preliminary determination of the structure of that from Eisenia Andrei at 4.7Å.

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Strand-Tibbitts, Kristen. "Crystallographic Studies of Rrythrocruorin from Lumbricus Terrestris: a Dissertation." eScholarship@UMMS, 2004. http://escholarship.umassmed.edu/gsbs_diss/309.

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The viability of multicellular aerobic organisms requires the binding and transport of molecular oxygen from the atmosphere to sites of metabolism. In the earthworm, Lumbricus terrestris, erythrocruorins are freely dissolved multi-subunit protein complexes that serve the same functions as red blood cells The aims of this study were to 1) determine the overall arrangement of hemoglobin chains and non-hemoglobin chains in Lumbricus erythrocruorin, 2) determine the stereochemical determinants specifying erythrocruorin's hierarchical symmetry, and 3) investigate the molecular and chemical basis for the remarkable cooperative binding of ligands to earthworm hemoglobin. Erythrocruorin is a highly cooperative oxygen-carrying protein with Hill coefficients measured at some pH's as high as n = 7.9. Crystallographic analysis of the whole erythrocruorin molecule structure to 5.5 Å resolution reveals a hierarchical organization of 144 oxygen-binding polypeptides and 36 non-hemoglobin linker polypeptide chains. The hemoglobin chains are arranged in a novel dodecameric substructure at the periphery of the complex, whereas 36 linker chains comprise the inner core and projected triple-stranded, helical coiled-coil spokes towards the center of the complex. Interdigitation of these spokes appears crucial for stabilizing the complex. Crystallographic analysis of crystals from isolated hemoglobin chains provides greater detail (resolution = 2.6 Å) and complete atomic models for the hemoglobin polypeptides. Comparison of these models with other hemoglobins reveal unique features in the distal heme pocket, including large aromatic residues at the B10 position in three of the four hemoglobin chains. Aromatic residues at this position have been implicated in other hemoglobins to confer resistance to oxidation. Molecular interactions across each subunit include pH-dependent interactions that are consistent with the observed Bohr effect on oxygen binding. Specifically a π-cation interaction between an arginine of one subunit to a histidine of the opposing subunit is likely an important molecular switch in the allosteric transition from a low to high affInity ligand-binding state.

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EL, IDRISSI SLITINE FOUZIA. "Etude structurale et fonctionnelle d'hemoglobines extracellulaires d'annelides (erythrocruorines)." Paris 6, 1991. http://www.theses.fr/1991PA066476.

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L'hemoglobine extracellulaire d'arenicola marina a ete purifiee. Son image au microscope electronique montre une structure hexagonale en deux etages, formee de 12 sous-multiples identiques. Sa masse moleculaire determinee par la diffusion des rayons x est 3 millions da et son phi est de 4,6. Cette proteine est composee de 6 types de chaines (a#1, a#2, b#1, b#2, c et d). Un modele d'architecture moleculaire a ete etabli sur la base des resultats d'electrophorese, de sequence n terminale ainsi que des resultats de la diffusion des rayons x. Les chaines a#2, b#1 et b#2 forment un trimere et sont reliees par des ponts disulfures. A ce trimere, la chaine a, est liee par des liaisons non covalentes pour former un tetramere. Trois tetrameres forment le douzieme de la molecule, les chaines c et d assurant la cohesion de l'ensemble de la proteine. Les chaines a#1, a#2, et b#1 presentent une homologie de sequence avec l'erythrocruorine d'un autre polychete, tylorrhynchus heterochaetus. On observe egalement la conservation de residus communs a la chaine beta de l'hemoglobine humaine et qui sont impliques dans le repliement de la structure secondaire de type myoglobine. L'erythrocruorine d'arenicole possede une forte affinite pour l'oxygene. La fixation et le transport de celui-ci se font avec une forte cooperativite entre les sous-unites. L'etude fonctionnelle de la proteine dissociee puis reassociee montre que, comme dans l'hemoglobine des vertebres, l'unite fonctionnelle de l'erythrocruorine d'arenicole, est un tetramere (a#1 (a#2, b#1, b#2))

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Elmer, Jacob James. "Expression, Purification, and Characterization of Mammalian and Earthworm Hemoglobins." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1321458620.

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Book chapters on the topic "Erythrocruorins"

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Zagra, Michela, Vincenza Mezzasalma, and Benedetto Salvato. "Structural Analogies in Annelid Erythrocruorins." In Invertebrate Oxygen Carriers. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_9.

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Vinogradov, S. N. "The Structure of Erythrocruorins and Chlorocruorins, the Invertebrate Extracellular Hemoglobins." In Respiratory Pigments in Animals. Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70616-5_2.

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Tsfadia, Y., and E. Daniel. "Subunit Structure of Earthworm Erythrocruorin." In Invertebrate Oxygen Carriers. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_4.

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Magaldi, A. Ghiretti, and G. Tognon. "Ophelia bicornis Erythrocruorin. Some Peculiar Features." In Invertebrate Oxygen Carriers. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_7.

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Chiancone, E., F. Ascoli, B. Giardina, R. Santucci, P. Vecchini, and D. Verzili. "Quaternary Structure and Modulation of Function in Earthworm Erythrocruorin." In Invertebrate Oxygen Carriers. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_15.

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Ilan, E., I. Hammel, M. M. David, and E. Daniel. "Quaternary Structure of Erythrocruorin from the Aquatic Snail Helisoma trivolvis." In Invertebrate Oxygen Carriers. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_17.

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Imai, K., S. Yoshikawa, K. Fushitani, H. Takizawa, T. Handa, and H. Kihara. "Inference of Allosteric Unit in Chlorocruorin, Erythrocruorin, and Hemerythrin on the Basis of the Monod-Wyman-Changeux Model." In Invertebrate Oxygen Carriers. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71481-8_61.

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